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Protein

Cysteine desulfurase, mitochondrial

Gene

NFS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.5 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.1 Publication

Cofactori

pyridoxal 5'-phosphateBy similarity

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei248 – 2481Pyridoxal phosphateBy similarity
Binding sitei276 – 2761Pyridoxal phosphateBy similarity
Binding sitei336 – 3361Pyridoxal phosphateBy similarity
Active sitei421 – 4211Cysteine persulfide intermediateBy similarity
Metal bindingi421 – 4211Iron-sulfur (2Fe-2S); via persulfide groupBy similarity

GO - Molecular functioni

  1. cysteine desulfurase activity Source: SGD
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: SGD
  2. cysteine metabolic process Source: InterPro
  3. iron-sulfur cluster assembly Source: SGD
  4. mitochondrial tRNA thio-modification Source: SGD
  5. tRNA thio-modification Source: SGD
  6. tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
ReactomeiREACT_327869. Mitochondrial iron-sulfur cluster biogenesis.
REACT_344671. Molybdenum cofactor biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase, mitochondrial1 Publication (EC:2.8.1.71 Publication)
Alternative name(s):
tRNA-splicing protein SPL11 Publication
Gene namesi
Name:NFS1Imported
Synonyms:SPL11 Publication
Ordered Locus Names:YCL017CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCL017c.
SGDiS000000522. NFS1.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. L-cysteine desulfurase complex Source: SGD
  2. mitochondrion Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Impairs cysteine desulfurase activity of mitochondria. Leads to strong accumulation of free iron, not bound to heme or Fe/S clusters, in mitochondria, as well as to decreased amounts of the mitochondrial Fe/S proteins including aconitase and succinate dehydrogenase. Leads also to accumulation of 5-methoxycarbonylmethyluridine (mcm5U) and a concomitant decrease in 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911I → S: Exhibits constitutive up-regulation of the genes of the cellular iron uptake system. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 497464Cysteine desulfurase, mitochondrialPRO_0000001304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP25374.
PaxDbiP25374.
PeptideAtlasiP25374.
PRIDEiP25374.

Expressioni

Gene expression databases

GenevestigatoriP25374.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ISD11Q6Q56010EBI-11991,EBI-784315
ISU1Q030202EBI-11991,EBI-29901

Protein-protein interaction databases

BioGridi30967. 21 interactions.
DIPiDIP-2948N.
IntActiP25374. 14 interactions.
MINTiMINT-474525.
STRINGi4932.YCL017C.

Structurei

3D structure databases

ProteinModelPortaliP25374.
SMRiP25374. Positions 99-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni168 – 1692Pyridoxal phosphate bindingBy similarity
Regioni296 – 2983Pyridoxal phosphate bindingBy similarity

Domaini

the N-terminal beta-strand formed by residues 99-104 is essential for the function.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1104.
GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
InParanoidiP25374.
KOiK04487.
OMAiAEKMMQC.
OrthoDBiEOG7ZKSMC.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKSTATRSI TRLSQVYNVP AATYRACLVS RRFYSPPAAG VKLDDNFSLE
60 70 80 90 100
THTDIQAAAK AQASARASAS GTTPDAVVAS GSTAMSHAYQ ENTGFGTRPI
110 120 130 140 150
YLDMQATTPT DPRVLDTMLK FYTGLYGNPH SNTHSYGWET NTAVENARAH
160 170 180 190 200
VAKMINADPK EIIFTSGATE SNNMVLKGVP RFYKKTKKHI ITTRTEHKCV
210 220 230 240 250
LEAARAMMKE GFEVTFLNVD DQGLIDLKEL EDAIRPDTCL VSVMAVNNEI
260 270 280 290 300
GVIQPIKEIG AICRKNKIYF HTDAAQAYGK IHIDVNEMNI DLLSISSHKI
310 320 330 340 350
YGPKGIGAIY VRRRPRVRLE PLLSGGGQER GLRSGTLAPP LVAGFGEAAR
360 370 380 390 400
LMKKEFDNDQ AHIKRLSDKL VKGLLSAEHT TLNGSPDHRY PGCVNVSFAY
410 420 430 440 450
VEGESLLMAL RDIALSSGSA CTSASLEPSY VLHALGKDDA LAHSSIRFGI
460 470 480 490
GRFSTEEEVD YVVKAVSDRV KFLRELSPLW EMVQEGIDLN SIKWSGH
Length:497
Mass (Da):54,467
Last modified:March 15, 2004 - v2
Checksum:iD709E326B3921BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501H → Y in AAA34814 (PubMed:8444805).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRiS19343.
RefSeqiNP_009912.2. NM_001178664.1.

Genome annotation databases

EnsemblFungiiYCL017C; YCL017C; YCL017C.
GeneIDi850343.
KEGGisce:YCL017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRiS19343.
RefSeqiNP_009912.2. NM_001178664.1.

3D structure databases

ProteinModelPortaliP25374.
SMRiP25374. Positions 99-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30967. 21 interactions.
DIPiDIP-2948N.
IntActiP25374. 14 interactions.
MINTiMINT-474525.
STRINGi4932.YCL017C.

Proteomic databases

MaxQBiP25374.
PaxDbiP25374.
PeptideAtlasiP25374.
PRIDEiP25374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCL017C; YCL017C; YCL017C.
GeneIDi850343.
KEGGisce:YCL017C.

Organism-specific databases

CYGDiYCL017c.
SGDiS000000522. NFS1.

Phylogenomic databases

eggNOGiCOG1104.
GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
InParanoidiP25374.
KOiK04487.
OMAiAEKMMQC.
OrthoDBiEOG7ZKSMC.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
ReactomeiREACT_327869. Mitochondrial iron-sulfur cluster biogenesis.
REACT_344671. Molybdenum cofactor biosynthesis.

Miscellaneous databases

NextBioi965791.
PROiP25374.

Gene expression databases

GenevestigatoriP25374.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing."
    Leong-Morgenthaler P.M., Kolman C., Oliver S.G., Hottinger H., Soell D.
    J. Bacteriol. 175:1433-1442(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Valles G., Volckaerts G.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 150.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Nucleotide sequence of the 3' terminal region of the LEU2 gene from Saccharomyces cerevisiae."
    Froman B.E., Tait R.C., Rodriguez R.L.
    Gene 31:257-261(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-497.
  6. "The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins."
    Kispal G., Csere P., Prohl C., Lill R.
    EMBO J. 18:3981-3989(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION.
  7. "Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution."
    Li J., Kogan M., Knight S.A., Pain D., Dancis A.
    J. Biol. Chem. 274:33025-33034(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF ILE-191.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs."
    Nakai Y., Umeda N., Suzuki T., Nakai M., Hayashi H., Watanabe K., Kagamiyama H.
    J. Biol. Chem. 279:12363-12368(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae."
    Muhlenhoff U., Balk J., Richhardt N., Kaiser J.T., Sipos K., Kispal G., Lill R.
    J. Biol. Chem. 279:36906-36915(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, DOMAIN.

Entry informationi

Entry nameiNFS1_YEAST
AccessioniPrimary (citable) accession number: P25374
Secondary accession number(s): D6VQZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: April 1, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.